6N9Q

Structure of the Quorum Quenching lactonase from Parageobacillus caldoxylosilyticus bind to substrate C4-AHL

6N9Q の概要

• エントリーDOI: 10.2210/pdb6n9q/pdb
• 関連するPDBエントリー: 6N9I
• 分子名称: Lactonase GcL, COBALT (II) ION, SULFATE ION, ... (10 entities in total)
• 機能のキーワード: lactonase; quorum sensing, thermophile, mll; quorum quenching; ahl., hydrolase
• 由来する生物種: Parageobacillus caldoxylosilyticus NBRC 107762
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68623.91

構造登録者

Bergonzi, C.,Schwab, M.,Elias, M. (登録日: 2018-12-03, 公開日: 2019-04-03, 最終更新日: 2023-10-11)

主引用文献

Bergonzi, C.,Schwab, M.,Naik, T.,Elias, M.
The Structural Determinants Accounting for the Broad Substrate Specificity of the Quorum Quenching Lactonase GcL.
Chembiochem, 20:1848-1855, 2019

PubMed Abstract: Quorum quenching lactonases are enzymes capable of hydrolyzing lactones, including N-acyl homoserine lactones (AHLs). AHLs are molecules known as signals in bacterial communication dubbed quorum sensing. Bacterial signal disruption by lactonases was previously reported to inhibit behavior regulated by quorum sensing, such as the expression of virulence factors and the formation of biofilms. Herein, we report the enzymatic and structural characterization of a novel lactonase representative from the metallo-β-lactamase superfamily, dubbed GcL. GcL is a broad spectrum and highly proficient lactonase, with k /K values in the range of 10 to 10  m  s . Analysis of free GcL structures and in complex with AHL substrates of different acyl chain length, namely, C4-AHL and 3-oxo-C12-AHL, allowed their respective binding modes to be elucidated. Structures reveal three subsites in the binding crevice: 1) the small subsite where chemistry is performed on the lactone ring; 2) a hydrophobic ring that accommodates the amide group of AHLs and small acyl chains; and 3) the outer, hydrophilic subsite that extends to the protein surface. Unexpectedly, the absence of structural accommodation for long substrate acyl chains seems to relate to the broad substrate specificity of the enzyme.

PubMed: 30864300
DOI: 10.1002/cbic.201900024

実験手法

X-RAY DIFFRACTION (2.35 Å)